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The enzyme '''UDP-glucose 4-epimerase''' (), also known as '''UDP-galactose 4-epimerase''' or '''GALE''', is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity. Additionally, human and some bacterial GALE isoforms reversibly catalyze the formation of UDP-''N''-acetylgalactosamine (UDP-GalNAc) from UDP-''N''-acetylglucosamine (UDP-GlcNAc) in the presence of NAD+, an initial step in glycoprotein or glycolipid synthesis.
Width| caption = ''H. sapiens'' UDP-glucose 4-epimerase homodimer bound to NADH and UDP-glucose. Domains: N-terminal and C-terminal.
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gale, zona, 1874-1938
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